Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Jorg Langowski"'
Publikováno v:
TASK Quarterly, Vol 18, Iss 3 (2014)
Histone N(C)-terminal tails play an important role in chromatin remodeling and gene regulation. Posttranslational modifications (PTMs) of histone tails are known to be correlated to distinct states of gene activity, but the molecular mechanism of the
Externí odkaz:
https://doaj.org/article/68a472bf60124397b61ae78e3b7e107b
Autor:
Konstantin V. Klenin, Katalin Tóth, Roland P. May, Nathalie Brun, Jorg Langowski, Markus Hammermann
Publikováno v:
Journal of Applied Crystallography. 33:526-529
We have measured the static form factor of superhelical DNA by SANS in dilute aqueous solution as a function of salt concentration. Theoretical static form factors were calculated by Monte Carlo simulations. Simulated and measured form factors are in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::09a78a0063333d73e30aa8e5e802d749
https://doi.org/10.1107/s0021889800099933
https://doi.org/10.1107/s0021889800099933
Autor:
Alexander Gansen, Suren Felekyan, Ralf Kühnemuth, Kathrin Lehmann, Katalin Tóth, Claus A. M. Seidel, Jörg Langowski
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
Nucleosomes compact the genome and regulate access to specific DNA sequences. Here the authors employ single-molecule FRET studies to characterize nucleosome dynamics at different salt concentrations and dissect nucleosome disassembly into elementary
Externí odkaz:
https://doaj.org/article/027c6235d43c47e7b8c91fcf0e44bef1
Autor:
Paul Victor Sauer, Jennifer Timm, Danni Liu, David Sitbon, Elisabetta Boeri-Erba, Christophe Velours, Norbert Mücke, Jörg Langowski, Françoise Ochsenbein, Geneviève Almouzni, Daniel Panne
Publikováno v:
eLife, Vol 6 (2017)
How the very first step in nucleosome assembly, deposition of histone H3-H4 as tetramers or dimers on DNA, is accomplished remains largely unclear. Here, we report that yeast chromatin assembly factor 1 (CAF1), a conserved histone chaperone complex t
Externí odkaz:
https://doaj.org/article/13159998535b4ce984485d81f26c20d9
Publikováno v:
PLoS ONE, Vol 11, Iss 6, p e0157451 (2016)
Intermediate filament (IF) elongation proceeds via full-width "mini-filaments", referred to as "unit-length" filaments (ULFs), which instantaneously form by lateral association of extended coiled-coil complexes after assembly is initiated. In a compa
Externí odkaz:
https://doaj.org/article/e703af79af67463c8d10897368918fa4
Autor:
Agata Pernuš, Jörg Langowski
Publikováno v:
PLoS ONE, Vol 10, Iss 4, p e0123070 (2015)
We collected mobility and interaction maps of c-Fos-eGFP and c-Jun-mRFP1 transcription factors within living cell nuclei. c-Fos dimerizes with c-Jun to form the transcription activator protein-1 (AP-1) which binds to the specific recognition site. To
Externí odkaz:
https://doaj.org/article/977bd2920d954e37982ed1aa14074700
Publikováno v:
PLoS ONE, Vol 8, Iss 4, p e57018 (2013)
Nucleosome structure and stability affect genetic accessibility by altering the local chromatin morphology. Recent FRET experiments on nucleosomes have given valuable insight into the structural transformations they can adopt. Yet, even if performed
Externí odkaz:
https://doaj.org/article/69f33354955b446789c99e5e94058708
Autor:
Ronan Broderick, Sivaramakrishnan Ramadurai, Katalin Tóth, Denisio M Togashi, Alan G Ryder, Jörg Langowski, Heinz Peter Nasheuer
Publikováno v:
PLoS ONE, Vol 7, Iss 4, p e35537 (2012)
Eukaryotic DNA replication is a dynamic process requiring the co-operation of specific replication proteins. We measured the mobility of eGFP-Cdc45 by Fluorescence Correlation Spectroscopy (FCS) in vivo in asynchronous cells and in cells synchronized
Externí odkaz:
https://doaj.org/article/047d8be4478e45f3a39ad306bcde3cf1
Publikováno v:
PLoS Computational Biology, Vol 7, Iss 12, p e1002279 (2011)
Histone tails play an important role in nucleosome structure and dynamics. Here we investigate the effect of truncation of histone tails H3, H4, H2A and H2B on nucleosome structure with 100 ns all-atom molecular dynamics simulations. Tail domains of
Externí odkaz:
https://doaj.org/article/ee750a33b4684ddda8f786a138b457b0
Autor:
Thomas Kühn, Teemu O Ihalainen, Jari Hyväluoma, Nicolas Dross, Sami F Willman, Jörg Langowski, Maija Vihinen-Ranta, Jussi Timonen
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e22962 (2011)
We introduce a new method for mesoscopic modeling of protein diffusion in an entire cell. This method is based on the construction of a three-dimensional digital model cell from confocal microscopy data. The model cell is segmented into the cytoplasm
Externí odkaz:
https://doaj.org/article/45966f16aa314dd2919ac0b530383fa0